Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization.

ABSTRACT: Bacteria are encapsulated by a peptidoglycan cell wall that is essential for their survival¹. During cell wall assembly, a lipid-linked disaccharide-peptide precursor called lipid II is polymerized and cross-linked to produce mature peptidoglycan. As lipid II is polymerized, nascent polymers remain membrane-anchored at one end, and the other end becomes cross-linked to the matrix^2-4. How bacteria release newly synthesized peptidoglycan strands from the membrane to complete the synthesis of mature peptidoglycan is a long-standing question. Here, we show that a Staphylococcus aureus cell wall hydrolase and a membrane protein that contains eight transmembrane helices form a complex that may function as a peptidoglycan release factor. The complex cleaves nascent peptidogl

SUBMITTER: Schaefer K 

PROVIDER: S-EPMC7755832 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature